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- PDB-8tcb: Structure of human C4b-binding protein alpha chain CCP domains 1 ... -

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Basic information

Entry
Database: PDB / ID: 8tcb
TitleStructure of human C4b-binding protein alpha chain CCP domains 1 and 2 in complex with the hypervariable region of group A Streptococcus M87 protein
Components
  • C4b-binding protein alpha chain
  • M protein
KeywordsIMMUNE SYSTEM / immune evasion / human complement
Function / homology
Function and homology information


regulation of opsonization / response to symbiotic bacterium / negative regulation of complement activation, classical pathway / T cell mediated immunity / complement activation, classical pathway / Regulation of Complement cascade / positive regulation of protein catabolic process / blood microparticle / innate immune response / RNA binding ...regulation of opsonization / response to symbiotic bacterium / negative regulation of complement activation, classical pathway / T cell mediated immunity / complement activation, classical pathway / Regulation of Complement cascade / positive regulation of protein catabolic process / blood microparticle / innate immune response / RNA binding / extracellular space / extracellular region / plasma membrane
Similarity search - Function
C4b-binding protein alpha, oligomerization domain / Oligomerization domain of C4b-binding protein alpha / M protein repeat / M protein repeat / : / Streptococcal M proteins C repeat profile. / : / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain ...C4b-binding protein alpha, oligomerization domain / Oligomerization domain of C4b-binding protein alpha / M protein repeat / M protein repeat / : / Streptococcal M proteins C repeat profile. / : / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily
Similarity search - Domain/homology
: / C4b-binding protein alpha chain / M protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Streptococcus pyogenes (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.69 Å
AuthorsMcGowan, M.A. / Kolesinski, P. / Ghosh, P.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)NIH R01 AI154149 United States
CitationJournal: J.Biol.Chem. / Year: 2024
Title: Conservation of C4BP-binding sequence patterns in Streptococcus pyogenes M and Enn proteins.
Authors: Kolesinski, P. / McGowan, M. / Botteaux, A. / Smeesters, P.R. / Ghosh, P.
History
DepositionJun 30, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 6, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: C4b-binding protein alpha chain
C: M protein
D: M protein
B: C4b-binding protein alpha chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,4305
Polymers53,3914
Non-polymers391
Water52229
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)43.176, 73.802, 190.398
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP22121
Space group name HallP22ab(z,x,y)
Symmetry operation#1: x,y,z
#2: x,-y,-z
#3: -x,y+1/2,-z+1/2
#4: -x,-y+1/2,z+1/2

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Components

#1: Protein C4b-binding protein alpha chain / C4bp / Proline-rich protein / PRP


Mass: 14163.894 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: C4BPA, C4BP / Production host: Escherichia coli (E. coli) / References: UniProt: P04003
#2: Protein M protein


Mass: 12531.667 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus pyogenes (bacteria) / Gene: emm / Production host: Escherichia coli (E. coli) / References: UniProt: Q6TLP8
#3: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 29 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.84 Å3/Da / Density % sol: 56.7 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 0.1 M sodium citrate, pH 4.8, 0.2 M KH2PO4, 25% w/v PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.98 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 5, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.69→68.81 Å / Num. obs: 17478 / % possible obs: 98.7 % / Redundancy: 6.8 % / Biso Wilson estimate: 54.92 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.09 / Rpim(I) all: 0.037 / Rrim(I) all: 0.097 / Net I/σ(I): 20.3
Reflection shellResolution: 2.69→2.82 Å / Redundancy: 3 % / Rmerge(I) obs: 0.953 / Mean I/σ(I) obs: 1.4 / Num. unique obs: 2045 / CC1/2: 0.452 / Rpim(I) all: 0.641 / Rrim(I) all: 1.155 / % possible all: 90.1

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Processing

Software
NameVersionClassification
XDSdata reduction
pointlessdata scaling
Aimlessdata scaling
PHASERphasing
PHENIX1.20.1_4487refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.69→68.81 Å / SU ML: 0.4636 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.1603
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2784 872 5.01 %
Rwork0.2353 16542 -
obs0.2375 17414 98.66 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 56.45 Å2
Refinement stepCycle: LAST / Resolution: 2.69→68.81 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2675 0 1 29 2705
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00372732
X-RAY DIFFRACTIONf_angle_d0.61863740
X-RAY DIFFRACTIONf_chiral_restr0.0327430
X-RAY DIFFRACTIONf_plane_restr0.0038490
X-RAY DIFFRACTIONf_dihedral_angle_d4.1576392
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.69-2.860.37431330.3492521X-RAY DIFFRACTION92.09
2.86-3.080.36211450.28372754X-RAY DIFFRACTION99.97
3.08-3.390.26851430.24732718X-RAY DIFFRACTION99.97
3.39-3.880.28311470.22342789X-RAY DIFFRACTION100
3.88-4.890.22811470.19052805X-RAY DIFFRACTION99.97
4.89-68.810.28581570.24272955X-RAY DIFFRACTION99.81
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
13.846591113163.157819801114.762922622583.13867756414.738180668495.154020180530.280891960766-0.229334518224-0.2489754405270.5056022561710.0102436295481-0.05185147912920.334909975474-0.190130704653-0.3564378517820.420038721242-0.0612807006263-0.06151047477660.399792590740.07195476745040.487962809828-10.70392416670.36158191822-38.0491643541
22.60676622596-0.5364999851923.723775190250.102116200926-1.266472272225.07282828889-0.3029588176190.1530812741310.1479595835760.12625379627-0.1847794144840.0551472133731-0.4372281919850.4003259977510.3993815766570.7049808002940.06648140982950.003228689103960.282819660692-0.003703343086040.4103484495370.503482321591-11.3269047356-44.3105631161
30.6962197347420.6291949497721.917370115191.541953152012.863026926446.75779643488-0.0234889057609-0.104701978442-0.08307969798830.3115950173-0.1952435623880.4331016137050.444346547953-0.3566118247080.3286564470810.4455309384280.03901543050270.09845415852250.347645802681-0.01351791988540.453659324930.719618590383-13.7748618772-34.0822505348
41.79045166064-0.473864664833-0.4281154420853.277270583620.01385969446166.33886151846-0.361343406510.00907325550642-0.149295390150.7830504284890.01810155439890.06513055496220.4486932555820.01282121417180.2977060162720.486758918217-0.005926254953110.01015209115550.213372941321-0.02463232151930.438886990759.73423316505-24.636288152-42.3971113476
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11(chain 'A' and resid 0 through 124)AA0 - 1241 - 122
22(chain 'C' and resid 46 through 125)CB46 - 1251 - 80
33(chain 'D' and resid 46 through 110)DC46 - 1101 - 65
44(chain 'B' and resid 1 through 122)AA00D1 - 1221 - 112

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